1992 Fiscal Year Final Research Report Summary
Purification of cholesterol gallstone inhibitory and promoting glycoproteins in bile and its clinical significance
| Project/Area Number |
03670383
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Gastroenterology
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| Research Institution | Jikei University School of Medicine |
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Principal Investigator |
AOYAMA Nankei Jikei Univ.School of Med.Research Assoc. 1st Depart. of Internal Med., 医学部, 助手 (60231106)
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| Co-Investigator(Kenkyū-buntansha) |
MIYAZAKI Hiroshi Jikei Univ.School of Med.Research Assoc. 1st Depart. of Internal Med., 医学部, 助手 (70192367)
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| Project Period (FY) |
1991 – 1992
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| Keywords | Cholesterol gallstone / Cholesterol nucleation / Helix pomatia lectin / Con A lectin / Promoter glycoprotein / Inhibitor glycoprotein / 糖蛋白 |
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| Research Abstract |
Presence of glycoproteins in human bile which promote or inhibit cholesterol crystal formation in bile has been reported by Holzbach, Groen et al,. Holzbach et al, has reported a new method of cholesterol nucleation and growth assay using spectrophotometer, which can semi-quantify the promoting or inhibitory effects of those glycoproteins on cholesterol crystal formation in bile. We purified glycoproteins by series of procedures using gel chromatography, affinity chromatography(Con A and Helix pomatia lectin columns), and HPLC (ion exchanger column). Promoting and inhibitory activity of purified glycoproteins from human bile was examined by using cholesterol nucleation and growth assay. As the results, glycoproteins which showed promoting activity on cholesterol crystal formation in bile were mainly found in Con A lectin bounding protein fraction and those showed inhibitory activity were found in Helix pomatia lectin bounding fraction.The glycoprotein fraction which exhibited promoting effect on the cholesterol crystal formation in bile contained four different proteins on SDS-PAGE electrophoresis whose molecular weights ranged from 30 kD to 120 Kd. These glycoproteins are under further purification.
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